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Protein

Bifunctional purine biosynthesis protein PurH

Gene

purH

Organism
Pelobacter propionicus (strain DSM 2379)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide = tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.UniRule annotation
IMP + H2O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.UniRule annotation

Pathwayi

GO - Molecular functioni

  1. IMP cyclohydrolase activity Source: UniProtKB-HAMAP
  2. phosphoribosylaminoimidazolecarboxamide formyltransferase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. 'de novo' IMP biosynthetic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transferase

Keywords - Biological processi

Purine biosynthesis

Enzyme and pathway databases

BioCyciPPRO338966:GHL0-2633-MONOMER.
UniPathwayiUPA00074; UER00133.
UPA00074; UER00135.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional purine biosynthesis protein PurHUniRule annotation
Including the following 2 domains:
Phosphoribosylaminoimidazolecarboxamide formyltransferaseUniRule annotation (EC:2.1.2.3UniRule annotation)
Alternative name(s):
AICAR transformylaseUniRule annotation
IMP cyclohydrolaseUniRule annotation (EC:3.5.4.10UniRule annotation)
Alternative name(s):
ATICUniRule annotation
IMP synthaseUniRule annotation
InosinicaseUniRule annotation
Gene namesi
Name:purHUniRule annotation
Ordered Locus Names:Ppro_2592
OrganismiPelobacter propionicus (strain DSM 2379)
Taxonomic identifieri338966 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesPelobacteraceaePelobacter
ProteomesiUP000006732 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 521521Bifunctional purine biosynthesis protein PurHPRO_1000057903Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi338966.Ppro_2592.

Structurei

3D structure databases

ProteinModelPortaliA1AS76.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

The IMP cyclohydrolase activity resides in the N-terminal region.UniRule annotation

Sequence similaritiesi

Belongs to the PurH family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0138.
HOGENOMiHOG000230372.
KOiK00602.
OMAiPCGVAEG.
OrthoDBiEOG6QCDFF.

Family and domain databases

Gene3Di3.40.140.20. 2 hits.
3.40.50.1380. 1 hit.
HAMAPiMF_00139. PurH.
InterProiIPR024051. AICAR_Tfase_dom.
IPR002695. AICARFT_IMPCHas.
IPR016193. Cytidine_deaminase-like.
IPR011607. MGS-like_dom.
[Graphical view]
PANTHERiPTHR11692. PTHR11692. 1 hit.
PfamiPF01808. AICARFT_IMPCHas. 1 hit.
PF02142. MGS. 1 hit.
[Graphical view]
PIRSFiPIRSF000414. AICARFT_IMPCHas. 1 hit.
SMARTiSM00798. AICARFT_IMPCHas. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view]
SUPFAMiSSF52335. SSF52335. 1 hit.
SSF53927. SSF53927. 1 hit.
TIGRFAMsiTIGR00355. purH. 1 hit.

Sequencei

Sequence statusi: Complete.

A1AS76-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKIKRALIS VSNKRGIIEF SKVLAGYGVE ILSTGGTAKL LRDSGVDVKD
60 70 80 90 100
VSEFTGFPEM LDGRVKTLHP KVHGGLLGMR GNPEHVAKMR EFGIENIDMV
110 120 130 140 150
VVNLYPFEAT VAKEGCLLVD AIENIDIGGP TMLRSAAKNY PDVTVLVDSV
160 170 180 190 200
DYATIVDEMR ENGGEVSAKT NFGLAVKAFQ HTAAYDGAIS NYLGARLGEG
210 220 230 240 250
VDPFPPTFTF QVRKSQELRY GENPQQSAAF YVERDQHEAS VATCHQIQGK
260 270 280 290 300
ELSYNNIADT DAALECVKQF TEGPTCVIVK HANPCGVAIG SSLLEAYDRA
310 320 330 340 350
YSTDPESAFG GIIACNRELD LETARAICER QFVEVIVAPT ASPEAVQVVS
360 370 380 390 400
SKKNVRLLVY GEWPQTVVPR LDFKRVTGGL LVQSADQELF KNLQVVTKRQ
410 420 430 440 450
PTPEELIDLQ FSWRVAKFVK SNAIVYGRDG MTIGVGAGQM SRVNSARIAA
460 470 480 490 500
IKAEHAGLVV EGAVMASDAF FPFRDGIDNA ASVGIRAVIQ PGGSMRDAEV
510 520
IAAADEHGMA MVFTGMRHFR H
Length:521
Mass (Da):56,449
Last modified:January 22, 2007 - v1
Checksum:i0DE49052151DD7E2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000482 Genomic DNA. Translation: ABL00197.1.
RefSeqiYP_902254.1. NC_008609.1.

Genome annotation databases

EnsemblBacteriaiABL00197; ABL00197; Ppro_2592.
KEGGippd:Ppro_2592.
PATRICi22898281. VBIPelPro64470_2746.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000482 Genomic DNA. Translation: ABL00197.1.
RefSeqiYP_902254.1. NC_008609.1.

3D structure databases

ProteinModelPortaliA1AS76.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi338966.Ppro_2592.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABL00197; ABL00197; Ppro_2592.
KEGGippd:Ppro_2592.
PATRICi22898281. VBIPelPro64470_2746.

Phylogenomic databases

eggNOGiCOG0138.
HOGENOMiHOG000230372.
KOiK00602.
OMAiPCGVAEG.
OrthoDBiEOG6QCDFF.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00133.
UPA00074; UER00135.
BioCyciPPRO338966:GHL0-2633-MONOMER.

Family and domain databases

Gene3Di3.40.140.20. 2 hits.
3.40.50.1380. 1 hit.
HAMAPiMF_00139. PurH.
InterProiIPR024051. AICAR_Tfase_dom.
IPR002695. AICARFT_IMPCHas.
IPR016193. Cytidine_deaminase-like.
IPR011607. MGS-like_dom.
[Graphical view]
PANTHERiPTHR11692. PTHR11692. 1 hit.
PfamiPF01808. AICARFT_IMPCHas. 1 hit.
PF02142. MGS. 1 hit.
[Graphical view]
PIRSFiPIRSF000414. AICARFT_IMPCHas. 1 hit.
SMARTiSM00798. AICARFT_IMPCHas. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view]
SUPFAMiSSF52335. SSF52335. 1 hit.
SSF53927. SSF53927. 1 hit.
TIGRFAMsiTIGR00355. purH. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Complete sequence of chromosome of Pelobacter propionicus DSM 2379."
    US DOE Joint Genome Institute
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F.
    , Land M., Hauser L., Kyrpides N., Kim E., Lovley D., Richardson P.
    Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: DSM 2379.

Entry informationi

Entry nameiPUR9_PELPD
AccessioniPrimary (citable) accession number: A1AS76
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 4, 2008
Last sequence update: January 22, 2007
Last modified: March 31, 2015
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.